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3P48

Structure of the yeast dUTPase DUT1 in complex with dUMPNPP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004170molecular_functiondUTP diphosphatase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006226biological_processdUMP biosynthetic process
A0009117biological_processnucleotide metabolic process
A0009213biological_processpyrimidine deoxyribonucleoside triphosphate catabolic process
A0016787molecular_functionhydrolase activity
A0035863biological_processdITP catabolic process
A0035870molecular_functiondITP diphosphatase activity
A0046081biological_processdUTP catabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004170molecular_functiondUTP diphosphatase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006226biological_processdUMP biosynthetic process
B0009117biological_processnucleotide metabolic process
B0009213biological_processpyrimidine deoxyribonucleoside triphosphate catabolic process
B0016787molecular_functionhydrolase activity
B0035863biological_processdITP catabolic process
B0035870molecular_functiondITP diphosphatase activity
B0046081biological_processdUTP catabolic process
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004170molecular_functiondUTP diphosphatase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006226biological_processdUMP biosynthetic process
C0009117biological_processnucleotide metabolic process
C0009213biological_processpyrimidine deoxyribonucleoside triphosphate catabolic process
C0016787molecular_functionhydrolase activity
C0035863biological_processdITP catabolic process
C0035870molecular_functiondITP diphosphatase activity
C0046081biological_processdUTP catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE DUP A 148
ChainResidue
AARG68
AHOH186
AHOH211
AHOH246
AHOH247
AHOH260
AHOH406
CLYS74
CALA81
CGLY82
CVAL83
ASER69
CASP85
CTYR88
CLYS93
AGLY70
AGLN114
AMG149
AHOH164
AHOH168
AHOH176
AHOH178

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 149
ChainResidue
ADUP148
AHOH168
AHOH246
AHOH247

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE DUP B 148
ChainResidue
AALA81
AGLY82
AVAL83
AASP85
ATYR88
AVAL92
ALYS93
BARG68
BSER69
BGLY70
BGLN114
BMG150
BHOH161
BHOH175
BHOH180
BHOH207
BHOH214
BHOH219
BHOH248
BHOH249
BHOH250
BHOH257
BHOH396

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DUP B 149
ChainResidue
BALA81
BGLY82
BVAL83
BASP85
BTYR88
BVAL92
BLYS93
BHOH190
BHOH225
BHOH234
BHOH276
BHOH377
CMET48
CARG68
CSER69
CGLY70
CGLN114
CMG148

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 150
ChainResidue
BDUP148
BHOH248
BHOH249
BHOH250

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 148
ChainResidue
BDUP149
BHOH276
CASP32

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21548881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3F4F","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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